| Literature DB >> 15094395 |
Robert Hamel1, Vasu D Appanna, Thammaiah Viswanatha, Simone Puiseux-Dao.
Abstract
Isocitrate lyase, ICL (EC 4.1.3.1), an enzyme that cleaves isocitrate into succinate, and glyoxylate appears to play a pivotal role in the detoxification of aluminum (Al) in Pseudomonas fluorescens. Here, we present evidence that the 4-fold increase in ICL activity observed in Al-stressed cells is due to the overexpression of this enzyme. Blue-Native-PAGE, Western blotting, and spectrophotometric experiments revealed that ICL is optimally expressed at 35 h of growth in Al-stressed cells. However, following the immobilization of Al, at 60 h of growth, the level of the enzyme decreases markedly. This enzyme that exists as a homotetramer with a molecular mass of approximately 133 kDa appears to be transcriptionally regulated. The overexpression of ICL may be a specific response to Al-stress as P. fluorescens grown in the presence of such metals as Ga3+, Pb2+, and Ca2+ does not undergo any significant increase in ICL activity. Thus, these findings support the notion that the overexpression of ICL plays a pivotal role in the survival and in the increased oxalogenesis observed in Al-stressed P. fluorescens.Entities:
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Year: 2004 PMID: 15094395 DOI: 10.1016/j.bbrc.2004.03.157
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN: 0006-291X Impact factor: 3.575